ArticleThe Journal of cell biology1997
Possible involvement of phosphorylation of occludin in tight junction formation.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.
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Who cites it
175 citing papers in PubMed, 576 citations in OpenAlex.
- Prostaglandin-induced cervical remodelling in humans in the first trimester is associated with increased expression of specific tight junction, but not gap junction proteins.Journal of translational medicine · 2012Trial
- Prophylactic C-terminal occludin-derived peptide attenuates LPS-induced airway inflammation via barrier preservation and mitochondrial ROS regulation.Redox biology · 2026Article
- Dietary Flavonoids as Cross-System Modulators of Hypertension and Intestinal Permeability.Molecules (Basel, Switzerland) · 2025Review
- Modulation of the blood-brain barrier permeability by patient-derived glioblastoma stem cell secretome.Scientific reports · 2025Article
- Article
- The Lego hypothesis of tissue morphogenesis: stereotypic organization of parallel orientational cell adhesions for epithelial self-assembly.Biological reviews of the Cambridge Philosophical Society · 2025Review
- Understanding the Blood-Brain Barrier: From Physiology to Pathology.Advances in experimental medicine and biology · 2025Review
- Cigarette smoke alters calcium flux to induce PP2A membrane trafficking and endothelial cell permeability.Scientific reports · 2024Article
- Intestinal Dysbiosis, Tight Junction Proteins, and Inflammation in Rheumatoid Arthritis Patients: A Cross-Sectional Study.International journal of molecular sciences · 2024Article
- Alkaline phosphatase treatment of acute kidney injury-an update.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2024Review
- EpCAM proteolysis and release of complexed claudin-7 repair and maintain the tight junction barrier.The Journal of cell biology · 2023Article
- Serine 408 phosphorylation is a molecular switch that regulates structure and function of the occludin α-helical bundle.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tight junction proteins occludin and ZO-1 as regulators of epithelial proliferation and survival.Annals of the New York Academy of Sciences · 2022Review
- Pathophysiological role of ion channels and transporters in gastrointestinal mucosal diseases.Cellular and molecular life sciences : CMLS · 2021Review
- Necrotizing Enterocolitis: Overview on In Vitro Models.International journal of molecular sciences · 2021Review
- Role of Barrier Integrity and Dysfunctions in Maintaining the Healthy Gut and Their Health Outcomes.Frontiers in physiology · 2021Review
- Tight Junctions of the Neurovascular Unit.Frontiers in molecular neuroscience · 2021Review
- Glucose but Not Fructose Alters the Intestinal Paracellular Permeability in Association With Gut Inflammation and Dysbiosis in Mice.Frontiers in immunology · 2021Article
- Expression of Tight Junction Proteins According to Functional Dyspepsia Subtype and Sex.Journal of neurogastroenterology and motility · 2020Article
- Sphingosine 1-Phosphate Signaling Is Involved in Impaired Blood-Brain Barrier Function in Ischemia-Reperfusion Injury.Molecular neurobiology · 2020Article
115 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Occludin is an integral membrane protein localizing at tight junctions in epithelial and endothelial cells. Occludin from confluent culture MDCK I cells resolved as several (>10) bands between 62 and 82 kD in SDS-PAGE, of which two or three bands of the lowest Mr were predominant. Among these bands, the lower predominant bands were essentially extracted with 1% NP-40, whereas the other higher Mr bands were selectively recovered in the NP-40-insoluble fraction. Alkaline phosphatase treatment converged these bands of occludin both in NP-40-soluble and -insoluble fractions into the lowest Mr band, and phosphoamino acid analyses identified phosphoserine (and phosphothreonine weakly) in the higher Mr bands of occludin. These findings indicated that phosphorylation causes an upward shift of occludin bands and that highly phosphorylated occludin resists NP-40 extraction. When cells were grown in low Ca medium, almost all occludin was NP-40 soluble. Switching from low to normal Ca medium increased the amount of NP-40-insoluble occludin within 10 min, followed by gradual upward shift of bands. This insolubilization and the band shift correlated temporally with tight junction formation detected by immunofluorescence microscopy. Furthermore, we found that the anti-chicken occludin mAb, Oc-3, did not recognize the predominant lower Mr bands of occludin (non- or less phosphorylated form) but was specific to the higher Mr bands (phosphorylated form) on immunoblotting. Immunofluorescence microscopy revealed that this mAb mainly stained the tight junction proper of intestinal epithelial cells, whereas other anti-occludin mAbs, which can recognize the predominant lower Mr bands, labeled their basolateral membranes (and the cytoplasm) as well as tight junctions. Therefore, we conclude that non- or less phosphorylated occludin is distributed on the basolateral membranes and that highly phosphorylated occludin is selectively concentrated at tight juctions as the NP-40-insoluble form. These findings suggest that the phosphorylation of occludin is a key step in tight junction assembly.
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